Fatty Acid Transfer Across the Myocardial Capillary Wall: No Evidence of a Substantial Role for Cytoplasmic Fatty Acid-binding Protein

It has recently been hypothesized that fatty acid (FA) transfer across the myocardial capillary wall is mediated by cytoplasmic fatty acid-binding protein (FABP). Therefore, we studied the type and content of FABP in endothelial cells from rat heart, using molecular biological, immunochemical, and F...

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Veröffentlicht in:Journal of molecular and cellular cardiology 1994-12, Vol.26 (12), p.1635-1647
Hauptverfasser: Van Nieuwenhoven, Frans A., Verstijnen, Cees P.H.J., Van Eys, Guillaume J.J.M., Van Breda, Eric, De Jong, Yvonne F., Van Der Vusse, Ger J., Glatz, Jan F.C.
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container_end_page 1647
container_issue 12
container_start_page 1635
container_title Journal of molecular and cellular cardiology
container_volume 26
creator Van Nieuwenhoven, Frans A.
Verstijnen, Cees P.H.J.
Van Eys, Guillaume J.J.M.
Van Breda, Eric
De Jong, Yvonne F.
Van Der Vusse, Ger J.
Glatz, Jan F.C.
description It has recently been hypothesized that fatty acid (FA) transfer across the myocardial capillary wall is mediated by cytoplasmic fatty acid-binding protein (FABP). Therefore, we studied the type and content of FABP in endothelial cells from rat heart, using molecular biological, immunochemical, and FA-binding assays. Studies were performed on short term cultured endothelial cells, two established endothelial cell lines and ultrathin cryosections from adult rat heart. Northern blotting analysis of endothelial cell RNA failed to detect either heart-type (H-) FABP or liver-type (L-) FABP mRNA, but the reversed transcription-polymerase chain reaction revealed both H- and L- FABP mRNAs, indicating the presence of minor amounts of these mRNAs. Highly sensitive immunochemical assays (sandwich ELISAs) using specific antibodies raised against rat H- or L-FABP showed the contents of these FABP-types in endothelial cells to be 1-5 ng/mg cytosolic protein, which is more than three orders of magnitude lower than the contents of H-FABP in heart or L-FABP in liver. Immuno-electron microscopy also showed that the concentration of H-FABP in endothelial cells is at least two orders of magnitude lower than that in cardiomyocytes. Finally, cytosolic protein samples from endothelial cells revealed no significant FA-binding activity in the 15-kDa region. We conclude that rat heart endothelial cells contain only minor quantities of cytoplasmic FABP and that, therefore, FA transport over the endothelium is mediated by FABP only to a minor extent. It is postulated that aqueous diffusion of FA through the endothelial cytoplasm most likely accounts for the experimentally observed rates of cardiac FA utilization.
doi_str_mv 10.1006/jmcc.1994.1183
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Immuno-electron microscopy also showed that the concentration of H-FABP in endothelial cells is at least two orders of magnitude lower than that in cardiomyocytes. Finally, cytosolic protein samples from endothelial cells revealed no significant FA-binding activity in the 15-kDa region. We conclude that rat heart endothelial cells contain only minor quantities of cytoplasmic FABP and that, therefore, FA transport over the endothelium is mediated by FABP only to a minor extent. 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Therefore, we studied the type and content of FABP in endothelial cells from rat heart, using molecular biological, immunochemical, and FA-binding assays. Studies were performed on short term cultured endothelial cells, two established endothelial cell lines and ultrathin cryosections from adult rat heart. Northern blotting analysis of endothelial cell RNA failed to detect either heart-type (H-) FABP or liver-type (L-) FABP mRNA, but the reversed transcription-polymerase chain reaction revealed both H- and L- FABP mRNAs, indicating the presence of minor amounts of these mRNAs. Highly sensitive immunochemical assays (sandwich ELISAs) using specific antibodies raised against rat H- or L-FABP showed the contents of these FABP-types in endothelial cells to be 1-5 ng/mg cytosolic protein, which is more than three orders of magnitude lower than the contents of H-FABP in heart or L-FABP in liver. Immuno-electron microscopy also showed that the concentration of H-FABP in endothelial cells is at least two orders of magnitude lower than that in cardiomyocytes. Finally, cytosolic protein samples from endothelial cells revealed no significant FA-binding activity in the 15-kDa region. We conclude that rat heart endothelial cells contain only minor quantities of cytoplasmic FABP and that, therefore, FA transport over the endothelium is mediated by FABP only to a minor extent. 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Verstijnen, Cees P.H.J. ; Van Eys, Guillaume J.J.M. ; Van Breda, Eric ; De Jong, Yvonne F. ; Van Der Vusse, Ger J. ; Glatz, Jan F.C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-70b88c96c49ca1c96ecc77852e104482ec4255ab5bfaf18c6ba104aad11cbe2f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological Transport - physiology</topic><topic>Blotting, Northern</topic><topic>Capillaries - metabolism</topic><topic>Carrier Proteins - metabolism</topic><topic>Cells, Cultured</topic><topic>Coronary Vessels - metabolism</topic><topic>Cytoplasm - metabolism</topic><topic>Diffusion</topic><topic>Endothelial cell</topic><topic>Endothelium, Vascular - metabolism</topic><topic>Fatty acid transfer</topic><topic>Fatty acid-binding protein</topic><topic>Fatty Acid-Binding Protein 7</topic><topic>Fatty Acid-Binding Proteins</topic><topic>Fatty Acids - metabolism</topic><topic>Immunohistochemistry</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Neoplasm Proteins</topic><topic>Nerve Tissue Proteins</topic><topic>Polymerase Chain Reaction</topic><topic>Rats</topic><topic>Rats, Inbred Lew</topic><topic>Rats, Wistar</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Nieuwenhoven, Frans A.</creatorcontrib><creatorcontrib>Verstijnen, Cees P.H.J.</creatorcontrib><creatorcontrib>Van Eys, Guillaume J.J.M.</creatorcontrib><creatorcontrib>Van Breda, Eric</creatorcontrib><creatorcontrib>De Jong, Yvonne F.</creatorcontrib><creatorcontrib>Van Der Vusse, Ger J.</creatorcontrib><creatorcontrib>Glatz, Jan F.C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular and cellular cardiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van Nieuwenhoven, Frans A.</au><au>Verstijnen, Cees P.H.J.</au><au>Van Eys, Guillaume J.J.M.</au><au>Van Breda, Eric</au><au>De Jong, Yvonne F.</au><au>Van Der Vusse, Ger J.</au><au>Glatz, Jan F.C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fatty Acid Transfer Across the Myocardial Capillary Wall: No Evidence of a Substantial Role for Cytoplasmic Fatty Acid-binding Protein</atitle><jtitle>Journal of molecular and cellular cardiology</jtitle><addtitle>J Mol Cell Cardiol</addtitle><date>1994-12-01</date><risdate>1994</risdate><volume>26</volume><issue>12</issue><spage>1635</spage><epage>1647</epage><pages>1635-1647</pages><issn>0022-2828</issn><eissn>1095-8584</eissn><abstract>It has recently been hypothesized that fatty acid (FA) transfer across the myocardial capillary wall is mediated by cytoplasmic fatty acid-binding protein (FABP). Therefore, we studied the type and content of FABP in endothelial cells from rat heart, using molecular biological, immunochemical, and FA-binding assays. Studies were performed on short term cultured endothelial cells, two established endothelial cell lines and ultrathin cryosections from adult rat heart. Northern blotting analysis of endothelial cell RNA failed to detect either heart-type (H-) FABP or liver-type (L-) FABP mRNA, but the reversed transcription-polymerase chain reaction revealed both H- and L- FABP mRNAs, indicating the presence of minor amounts of these mRNAs. Highly sensitive immunochemical assays (sandwich ELISAs) using specific antibodies raised against rat H- or L-FABP showed the contents of these FABP-types in endothelial cells to be 1-5 ng/mg cytosolic protein, which is more than three orders of magnitude lower than the contents of H-FABP in heart or L-FABP in liver. Immuno-electron microscopy also showed that the concentration of H-FABP in endothelial cells is at least two orders of magnitude lower than that in cardiomyocytes. Finally, cytosolic protein samples from endothelial cells revealed no significant FA-binding activity in the 15-kDa region. We conclude that rat heart endothelial cells contain only minor quantities of cytoplasmic FABP and that, therefore, FA transport over the endothelium is mediated by FABP only to a minor extent. It is postulated that aqueous diffusion of FA through the endothelial cytoplasm most likely accounts for the experimentally observed rates of cardiac FA utilization.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>7731058</pmid><doi>10.1006/jmcc.1994.1183</doi><tpages>13</tpages></addata></record>
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subjects Animals
Base Sequence
Biological Transport - physiology
Blotting, Northern
Capillaries - metabolism
Carrier Proteins - metabolism
Cells, Cultured
Coronary Vessels - metabolism
Cytoplasm - metabolism
Diffusion
Endothelial cell
Endothelium, Vascular - metabolism
Fatty acid transfer
Fatty acid-binding protein
Fatty Acid-Binding Protein 7
Fatty Acid-Binding Proteins
Fatty Acids - metabolism
Immunohistochemistry
Male
Molecular Sequence Data
Neoplasm Proteins
Nerve Tissue Proteins
Polymerase Chain Reaction
Rats
Rats, Inbred Lew
Rats, Wistar
title Fatty Acid Transfer Across the Myocardial Capillary Wall: No Evidence of a Substantial Role for Cytoplasmic Fatty Acid-binding Protein
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